1JXU

CRAMBIN MIXED SEQUENCE FORM AT 240 K. PROTEIN/WATER SUBSTATES

Summary for 1JXU

• Entry DOI: 10.2210/pdb1jxu/pdb
• Related: 1JXW 1JXX 1JXY 1ab1 1cbn 1cnr 1crn 1ejg 1jxt
• Descriptor: Crambin, ETHANOL (2 entities in total)
• Functional Keywords: water, substate, function, plant protein
• Biological source: Crambe hispanica subsp. abyssinica
• Cellular location: Secreted: P01542
• Total number of polymer chains: 1
• Total formula weight: 4774.48

Authors

Teeter, M.M.,Yamano, A.,Stec, B.,Mohanty, U. (deposition date: 2001-09-09, release date: 2001-10-31, Last modification date: 2024-10-30)

Primary citation

Teeter, M.M.,Yamano, A.,Stec, B.,Mohanty, U.
On the nature of a glassy state of matter in a hydrated protein: Relation to protein function.
Proc.Natl.Acad.Sci.USA, 98:11242-11247, 2001

PubMed Abstract: Diverse biochemical and biophysical experiments indicate that all proteins, regardless of size or origin, undergo a dynamic transition near 200 K. The cause of this shift in dynamic behavior, termed a "glass transition," and its relation to protein function are important open questions. One explanation postulated for the transition is solidification of correlated motions in proteins below the transition. We verified this conjecture by showing that crambin's radius of gyration (Rg) remains constant below approximately 180 K. We show that both atom position and dynamics of protein and solvent are physically coupled, leading to a novel cooperative state. This glassy state is identified by negative slopes of the Debye-Waller (B) factor vs. temperature. It is composed of multisubstate side chains and solvent. Based on generalization of Adam-Gibbs' notion of a cooperatively rearranging region and decrease of the total entropy with temperature, we calculate the slope of the Debye-Waller factor. The results are in accord with experiment.

PubMed: 11572978
DOI: 10.1073/pnas.201404398

Experimental method

X-RAY DIFFRACTION (0.99 Å)